Abstract

The excitation wavelength dependence of the initial electron transfer rate in both wild type and mutant reaction centers from Rhodobacter sphaeroides has been studied between 840 and 920 nm as a function of temperature (10-295 K). The dynamics of primary charge separation show no resolvable excitation wavelength dependence at room temperature over this spectral range. A small variation in rate with excitation wavelength is observed at cryogenic temperatures. The low temperature results cannot be explained in terms either of a nonequilibrium model that assumes that the primary charge separation starts from a vibrationally hot state or a model that assumes a static inhomogeneous distribution of electron transfer driving forces. Instead these results are consistent with the concept that primary charge separation kinetics are controlled by the dynamics of protein conformational diffusion.

Original languageEnglish (US)
Pages (from-to)14296-14301
Number of pages6
JournalJournal of Physical Chemistry B
Volume112
Issue number45
DOIs
StatePublished - Nov 13 2008

Fingerprint

polarization (charge separation)
Wavelength
electron transfer
wavelengths
excitation
cryogenic temperature
Temperature
Electrons
Cryogenics
proteins
kinetics
room temperature
Proteins
Kinetics
temperature

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Excitation wavelength dependence of primary charge separation in reaction centers from rhodobacter Sphaeroides. / Wang, Haiyu; Lin, Su; Woodbury, Neal.

In: Journal of Physical Chemistry B, Vol. 112, No. 45, 13.11.2008, p. 14296-14301.

Research output: Contribution to journalArticle

@article{b5e47e2ba0074ed18d8f0a979ee7d4da,
title = "Excitation wavelength dependence of primary charge separation in reaction centers from rhodobacter Sphaeroides",
abstract = "The excitation wavelength dependence of the initial electron transfer rate in both wild type and mutant reaction centers from Rhodobacter sphaeroides has been studied between 840 and 920 nm as a function of temperature (10-295 K). The dynamics of primary charge separation show no resolvable excitation wavelength dependence at room temperature over this spectral range. A small variation in rate with excitation wavelength is observed at cryogenic temperatures. The low temperature results cannot be explained in terms either of a nonequilibrium model that assumes that the primary charge separation starts from a vibrationally hot state or a model that assumes a static inhomogeneous distribution of electron transfer driving forces. Instead these results are consistent with the concept that primary charge separation kinetics are controlled by the dynamics of protein conformational diffusion.",
author = "Haiyu Wang and Su Lin and Neal Woodbury",
year = "2008",
month = "11",
day = "13",
doi = "10.1021/jp8058799",
language = "English (US)",
volume = "112",
pages = "14296--14301",
journal = "Journal of Physical Chemistry B Materials",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "45",

}

TY - JOUR

T1 - Excitation wavelength dependence of primary charge separation in reaction centers from rhodobacter Sphaeroides

AU - Wang, Haiyu

AU - Lin, Su

AU - Woodbury, Neal

PY - 2008/11/13

Y1 - 2008/11/13

N2 - The excitation wavelength dependence of the initial electron transfer rate in both wild type and mutant reaction centers from Rhodobacter sphaeroides has been studied between 840 and 920 nm as a function of temperature (10-295 K). The dynamics of primary charge separation show no resolvable excitation wavelength dependence at room temperature over this spectral range. A small variation in rate with excitation wavelength is observed at cryogenic temperatures. The low temperature results cannot be explained in terms either of a nonequilibrium model that assumes that the primary charge separation starts from a vibrationally hot state or a model that assumes a static inhomogeneous distribution of electron transfer driving forces. Instead these results are consistent with the concept that primary charge separation kinetics are controlled by the dynamics of protein conformational diffusion.

AB - The excitation wavelength dependence of the initial electron transfer rate in both wild type and mutant reaction centers from Rhodobacter sphaeroides has been studied between 840 and 920 nm as a function of temperature (10-295 K). The dynamics of primary charge separation show no resolvable excitation wavelength dependence at room temperature over this spectral range. A small variation in rate with excitation wavelength is observed at cryogenic temperatures. The low temperature results cannot be explained in terms either of a nonequilibrium model that assumes that the primary charge separation starts from a vibrationally hot state or a model that assumes a static inhomogeneous distribution of electron transfer driving forces. Instead these results are consistent with the concept that primary charge separation kinetics are controlled by the dynamics of protein conformational diffusion.

UR - http://www.scopus.com/inward/record.url?scp=57049092194&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=57049092194&partnerID=8YFLogxK

U2 - 10.1021/jp8058799

DO - 10.1021/jp8058799

M3 - Article

VL - 112

SP - 14296

EP - 14301

JO - Journal of Physical Chemistry B Materials

JF - Journal of Physical Chemistry B Materials

SN - 1520-6106

IS - 45

ER -